Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.5.2 (NQO1)
 6,196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Tendon tissue of eleven athletes suffering from insertion tendopathy and of two controls was examined. Part of the tissue was prepared for routine light microscopy, a part for enzyme histochemical staining of Nicotinamide-adenine-dinudeotide-diaphorase (NADP-diaphorase), lactate dehydrogenase (LDH), beta-glucuronidase and alkaline phosphatase. Small pieces of tissue were also prepared for electron microscopic examination. The removed tissue was edematous and mushy. The normally densely packed parallel or interwoven collagen bundles were loosened by edema, focal necrosis or hemorrhage. Infiltration of fatty tissue and granulation tissue was also present. The amount of acid mucopolysaccharides was markedly increased. The histochemical studies showed strong enzyme activity of NADP-diaphorase and LDH in normal tendon tissue as well as around areas of degeneration and in granulation tissue. beta-Glucuronidase and alkaline phosphatase was present, but in general with lesser activity than the above enzymes. The electron microscopic examination revealed marked degeneration of the fiber systems, focal necrosis, deposit of amorphous masses and mucopolysaccharides and focal mineralisation. The reparative zones showed proliferating capillaries, often with a collapsed lumen and prominent endothelial cells and basement membranes.
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PMID:Insertion tendopathy in athletes. A light microscopic, histochemical and electron microscopic examination. 712 23

The preparation of affinity adsorbents for menadione reductase (EC 1.6.99.2), using CNBr-activated Sepharose 4B and activated CH-Sepharose 4B, is described. The adsorbents used are the sepharoses modified by 4-anilino-5-methoxybenzoquinone-1,2. Bound menadione reductase is specifically eluted with NAD(P)H, while NAD(P) has no effect on the enzyme. The enzyme yield of 83--95% and a 102-fold purification are achieved. Disc-electrophoresis reveals one protein fraction identified with menadione reductase and a separate inactive fraction. It is assumed that the specific binding of menadione reductase to the adsorbent is due to the formation of a complex between the oxidized enzyme and the quinone. This complex breaks down in the presence of NAD(P)H.
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PMID:[Affinity chromatography of menadione reductase]. 721 37

The purification by affinity chromatography up to homogeneity and the properties of NAD-reductase from purple sulfur bacterium Thiocapsa roseopersicina, strain BBS, are described. The molecular weight of NAD-reductase is about 80000; pI is 3.9. The enzyme consists of two subunits. According to the stabilizing effect of FAD at preparative electrophoresis and the inhibitory effect of atebrine NAD-reductase is a flavoprotein. The bulk of the enzyme (about 75%) is localized in the cell periplasmic space. NAD-reductase is less thermostable and has a lower O2 stability as compared to the NADP-reductase from the same organism. The enzyme is specific to NADH ane catalyzes the menadione-reductase reaction, diaphorase reaction of benzyl viologen and methyl viologen reductions. In the presence of NADH NAD-reductase reduces cytochromes c552 and "c3" from T. roseopersicina and forms a complex with spinach ferredoxin.
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PMID:[Purification and properties of NAD-reductase from phototrophic bacterium Thiocapsa roseopersicina]. 723 99

The quantitative cytochemical investigation of the prodigiozan effect on the enzymatic activity of the peritoneal macrophages was performed on mice. The drug was administered in a single dose of 150 microgram/kg 24 hours before the specimen collection. Prodigiozan promoted a reliable increase in the activity of the enzymes participating in glycolysis (lactate and cytoplasmic alpha-glycerophosphate dehydrogenases), hexoso-monophosphatic pathway of glucose oxidation (glucoso-6-phosphate dehydrogenase), succinate dehydrogenase, NADP. N-diaphorase and lysosomal enzymes, such as acid phosphatase and non-specific alpha-naphthyl acetate esterase. The changes indicate that activation of the macrophages is one of the significant mechanisms of increasing the host nonspecific resistance with prodigiozan.
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PMID:[Prodigiozan as an activator of peritoneal macrophages]. 727 Dec 60

D-Lactate dehydrogenase, the starting enzyme for carbon and energy metabolism in dissimilatory sulfate-reducing bacteria, has been purified 36-fold from the soluble fraction of the sonicate of Desulfovibrio vulgaris, Miyazaki. The enzyme is specific for D-lactate (Km = 0.8 mM) and DL-2-hydroxybutyrate (probably its D-isomer) as the electron donor substrate. It reduces, in the presence of lactate, various artificial electron acceptors such as 1-methoxyphenazinium methyl sulfate, ferricyanide, tetrazolium dyes, methylene blue, and 2,6-dichlorophenol-indophenol. When 2 mol of ferricyanide was reduced, 1 mol of pyruvate was produced during the reaction. Among natural electron carriers, only cytochrome c-553 isolated from the same organism can be reduced by the enzyme. The ferric complex of pyridine-2,6-dicarboxylate can act as an electron acceptor if cytochrome c-553 is present in the reaction system. NAD+, NADP+, FAD, FMN, cytochrome c3, high-molecular-weight cytochrome, eucaryotic cytochromes c (yeast and horse) and O2 could not be reduced. The enzyme does not have any diaphorase activity. The D-lactate dehydrogenase of D. vulgaris must therefore be named D-lactate:ferricytochrome c-553 oxidoreductase [EC subclass 1.1.2]. A similar enzyme exists in the formate dehydrogenase-less mutant of D. vulgaris, Miyazaki, and in D. vulgaris, Hildenborough.
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PMID:D-lactate dehydrogenase of Desulfovibrio vulgaris. 727 46

The flavoprotein NADP+ reductase from spinach chloroplasts may form a ternary complex with one molecule of NADP+ and one molecule of ferredoxin. Spectroscopic titration studies show that the NADP+ binding site and the ferredoxin binding site are totally independent, that is previous binding of ferredoxin does not modify binding of NADP+, and conversely. Since NADP+ reductase conditions the diaphorase reaction, that is an electron transfer between NADPH and various acceptors such as ferricyanide, the binding of ferrocyanide and its possible interaction with NADP+ and ferredoxin has been studied. Ferrocyanide behaves as a competitive inhibitor with respect to both NADP+ and ferredoxin. This seems paradoxical since NADP+ and ferredoxin are independently bound at two different non-overlapping sites of the flavoprotein. This apparent paradox may be resolved by a theoretical analysis of the interactions between either ferrocyanide and NADP+, or ferrocyanide and ferredoxin. Theory shows that if ferrocyanide is non-specifically bound at two independent sites, namely the NADP+ and the ferredoxin binding sites, it appears competitive with respect to both NADP+ and ferredoxin, although ternary flavoprotein-ferredoxin-ferrocyanide and flavoprotein-NADP+-ferrocyanide complexes are formed. The binding constants of NADP+, ferredoxin and ferrocyanide for the enzyme have been determined. These results are discussed in connection with the possible mechanism of the diaphorase reaction.
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PMID:Complex-forming properties of spinach NADP+ reductase with ferredoxin, ferrocyanide and NADP+. 740 54

Findings reported here show that there is a significant increase in the number of neurons in the pedunculopontine nucleus in most schizophrenic patients compared to age-matched controls. Nicotinamide adenine dinucleotide phosphate diaphorase histochemistry was used to label putative cholinergic neurons in the pedunculopontine nucleus and laterodorsal tegmental nucleus, while noradrenergic locus coeruleus neurons were labeled immunocytochemically using an antibody to tryosine hydroxylase. Cell counts of these neuronal groups were carried out using a Biographics image analysis system. We found significantly increased cell numbers in the pedunculopontine nucleus of schizophrenic patients compared to controls. The number of laterodorsal tegmental nucleus neurons was increased but this was not statistically significant. However, the total cell counts for pedunculopontine and laterodorsal tegmental nuclei were significantly higher in schizophrenic subjects. The number of locus coeruleus noradrenergic neurons was similar in both groups. These results implicate the brainstem reticular formation as a pathophysiological site in at least some patients with schizophrenia. In addition, these findings suggest a developmental etiology for the disease and account for some, but not all, of the symptoms of schizophrenia, including sensory gating abnormalities, sleep-wake disturbances and, perhaps, hallucinations. Overdriving of thalamic and substantia nigra function by cholinergic afferents from the midbrain may account for some of the symptoms seen in schizophrenia. These findings suggest that, at least in some schizophrenic patients, there is an increased number of neurons in the cholinergic arm of the reticular activating system. This may explain some of the symptoms of schizophrenia and points to a prenatal disturbance as one of the possible causes of the disease.
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PMID:Mesopontine neurons in schizophrenia. 747 75

These experiments were designed to examine the distribution of galanin-like peptide immunoreactivity (GAL-IR) in bullfrog sympathetic preganglionic neurons and to identify the peripheral target organs affected by these neurons. Cells expressing GAL-IR were observed in the intermediolateral column of segments 7 and 8 only. Apparent GAL-IR innervation is present, but rare, in sympathetic chain ganglia. Double-labelling with retrogradely transported fast blue and galanin antiserum demonstrated that most GAL-IR neurons project via splanchnic nerves to innervate the adrenal gland, which receives a dense plexus of GAL-IR fibers surrounding chromaffin cells. The adrenal gland is also innervated by preganglionic neurons in segments 5 and 6 that do not express GAL-IR. Because nitric oxide is expressed in sympathoadrenal preganglionic neurons in mammals (Anderson, C.R., Neurosci. Lett., 139 (1992) 280), we examined whether it is expressed in bullfrog preganglionic neurons. Nicotinamide adenine dinucleotide phosphate-diaphorase positive neurons are present in bullfrog spinal grey at segments 5 through 8. These neurons were not double-labelled with fast blue retrogradely transported from the sympathetic chain, celiac ganglion, or adrenal gland; nor were they double-labelled with GAL-antiserum. Thus nitric oxide is apparently not expressed in bullfrog sympathetic preganglionic neurons.
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PMID:Segmental restriction and target specificity of bullfrog preganglionic neurons that exhibit galanin-like immunoreactivity. 750 58

Nicotinamide adenine dinucleotide phosphate diaphorase (NADPHd) histochemistry was used as a marker for neuronal nitric oxide synthase in human bladder tissue. A plexus of NADPHd-containing nerve fibres was observed in bladder biopsies taken from both the lateral wall and trigone regions. Varicose terminals were present in smooth muscle bundles of the detrusor and trigone, and more commonly within the submucosal layer. Reactive fibres were seen running immediately beneath and along the urothelium, and additional nerves formed perivascular plexi around some blood vessels. Fewer positive nerve processes were observed in the trigone region in comparison to the bladder wall. NADPHd-reactive neuronal perikarya were present within intramural ganglia, some of which were in close proximity to NADPHd-stained varicosities. The results indicate that nitric oxide may be involved in the regulation of bladder function in humans.
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PMID:Distribution of NADPH-diaphorase-positive nerves supplying the human urinary bladder. 751 21

Nicotinamide-adenine dinucleotide phosphate-diaphorase (NADPH-d) positive cells were demonstrated in the medulla of the rat and chick thymus at light microscopic level. The NADPH-d positive cells were present as clusters and were predominantly localized near the corticomedullary boundary. These clusters were closely associated with the thymic cysts. Some cells were seen in close proximity to blood vessels. The presence of nitric oxide (NO) as indicated by the positive NADPH-d reaction in the cells forming the wall of the thymic cyst suggests a modulatory influence of NO over the activities of these cells. Other possible functions of NO are also discussed.
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PMID:NADPH-diaphorase positive cells in the chick and rat thymus. 751 99


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